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Ann E. McDermott

Researcher at Columbia University

Publications -  169
Citations -  9383

Ann E. McDermott is an academic researcher from Columbia University. The author has contributed to research in topics: Solid-state nuclear magnetic resonance & Magic angle spinning. The author has an hindex of 54, co-authored 163 publications receiving 8716 citations. Previous affiliations of Ann E. McDermott include University of Washington & Stony Brook University.

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The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis

TL;DR: Insight is provided into the structural changes that occur when RIP kinases are triggered to execute different signaling outcomes and the realm of amyloids is expanded to complex formation and signaling.
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Structure and Dynamics of Membrane Proteins by Magic Angle Spinning Solid-State NMR

TL;DR: This review highlights recent applications to intrinsic membrane proteins and summarizes recent technical advances that will enable these methods to be utilized for more complex membrane protein systems in the near future.
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Nuclear Magnetic Resonance Studies of Biopolymer Dynamics

TL;DR: This review describes NMR spectroscopic methods for investigation of conformational dynamics together with theoretical descriptions appropriate for interpretation and simulation of the techniques, surveys the range of results available from solution and solid state NMR studies of proteins and other biomolecules, and identifies opportunities for further individual and collaborative development of solution andSolid State NMR techniques for characterizing the dynamical properties of biological macromolecules.
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Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state.

TL;DR: It is demonstrated that high-resolution multidimensional solid state NMR methods can be used to correlate many backbone and side chain chemical shifts for hydrated micro-crystalline U-13C,15N Basic Pancreatic Trypsin Inhibitor.
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Determination of membrane protein structure by rotational resonance NMR : bacteriorhodopsin

TL;DR: Rotationally resonant magnetization exchange was used to determine the distance between the C-8 and C-18 carbons of retinal in two model compounds and in the membrane protein bacteriorhodopsin, illustrating that rotational resonance can be used for structural studies in membrane proteins and in other situations where diffraction and solution NMR techniques yield limited information.